Biological sciences

A recombinant form of the dye-decolorizing peroxidase DyP from Geotrichum candidum Dec 1 is 42 times more active when expressed in Aspergillus oryzae. The recombinant form is created by fusing the dyp gene with the A. oryzae alpha-amylase promotor amyB.

A new strain of Xanthomonas sp., termed strain DY44, capable of degrading hydrogen sulfide was recently isolated from peat. This heterotrophic bacteria requires the presence of oxygen to remove hydrogen sulfide from hydrogen-containing gases. This capability is specific to this strain and appears to be part of the cell's physiologic detoxification process. Despite having a lower hydrogen sulfide removal rate, DY44 can be cultured easily. It is therefore more efficient as a hydrogen sulfide remover than commonly used autotrophic bacteria.

Purification and characterization of a novel peroxidase from Geotrichum candidum Dec 1 involved in decolorization of dyes

Article Abstract:

The novel peroxidase DyP from Geotrichum candidum Dec 1 that is involved in the decolorization of dyes has been isolated and studied. G. candidum is a newly-isolated fungus that can decolorize 21 types of dyes including azo and anthraquinone dyes. DyP is a glycoprotein with a molecular mass of 60 kDa and an isoelectric point of 3.8. Its absorption spectrum exhibits a Soret band of 406 nm and its Na2S2O4-reduced form has a peak at 556 nm. DyP can also oxidize 2,6-dimethoxyphenol and guaiacol but not veratryl alcohol.